ID A0A1X7R7K1_9SACH Unreviewed; 476 AA.
AC A0A1X7R7K1;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=acid phosphatase {ECO:0000256|ARBA:ARBA00012646};
DE EC=3.1.3.2 {ECO:0000256|ARBA:ARBA00012646};
GN ORFNames=KASA_0K02926G {ECO:0000313|EMBL:SMN21615.1};
OS Kazachstania saulgeensis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kazachstania.
OX NCBI_TaxID=1789683 {ECO:0000313|EMBL:SMN21615.1, ECO:0000313|Proteomes:UP000196158};
RN [1] {ECO:0000313|EMBL:SMN21615.1, ECO:0000313|Proteomes:UP000196158}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a phosphate monoester + H2O = an alcohol + phosphate;
CC Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.2;
CC Evidence={ECO:0000256|ARBA:ARBA00000032};
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC {ECO:0000256|ARBA:ARBA00005375}.
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DR EMBL; FXLY01000008; SMN21615.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X7R7K1; -.
DR STRING; 1789683.A0A1X7R7K1; -.
DR OrthoDB; 2404758at2759; -.
DR Proteomes; UP000196158; Unassembled WGS sequence.
DR GO; GO:0003993; F:acid phosphatase activity; IEA:UniProtKB-EC.
DR CDD; cd07061; HP_HAP_like; 1.
DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR InterPro; IPR033379; Acid_Pase_AS.
DR InterPro; IPR000560; His_Pase_clade-2.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR016274; Histidine_acid_Pase_euk.
DR PANTHER; PTHR20963:SF18; ACID PHOSPHATASE PHO11-RELATED; 1.
DR PANTHER; PTHR20963; MULTIPLE INOSITOL POLYPHOSPHATE PHOSPHATASE-RELATED; 1.
DR Pfam; PF00328; His_Phos_2; 1.
DR PIRSF; PIRSF000894; Acid_phosphatase; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR PROSITE; PS00778; HIS_ACID_PHOSPHAT_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR000894-2};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000196158};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..476
FT /note="acid phosphatase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013185930"
FT ACT_SITE 79
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-1"
FT ACT_SITE 344
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-1"
FT DISULFID 68..393
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT DISULFID 268..281
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT DISULFID 418..426
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
SQ SEQUENCE 476 AA; 53357 MW; 714F121DB068FB5F CRC64;
MLNQILTLAS IASTASIVRA VAIDSAFLEN DFSKIGSQED IYQYLYGSAP HFSYPVNNSI
SLDIPETCEL VQVHLYARHG ERYPTAGSTA DGINNIWYKF GNYTQQFNGS LAFLNENYQY
PFANSSNYGL LTTPDNVANP YNPLLGSTTG TTEGLEFLEL YSNILHKHEN FTAWTSNSDR
VHATAEYFIR ALGDKFNVNL QTISEDASQG ANTLTPINGC PNWNETATTA ILAKYDQTFL
TDISKRLNAE NVGLNLTKTD ALNMFNWCAF EINVRGYSDI CDVFTKDELI KYGYYGDLMT
YYDEFIGNPL AKAVGSVPVN ATLALLNTPE DKLDQQVFLS FTHDTNLINY AAALGIFTDN
APITPESIDW TTDFHRSWLV PQGARIQTQK YNCKSPNNTS ISYVRFIVND VVKPLTNCSS
GPGFSCSLPD YNKFVEDRFQ DVDFYTQCGT SKVSNVTDLT FYWDYKTHDY NAPLEI
//
